ID HISX_CHRVO Reviewed; 434 AA. AC Q7P0F6; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 25-NOV-2008, entry version 43. DE RecName: Full=Histidinol dehydrogenase; DE Short=HDH; DE EC=1.1.1.23; GN Name=hisD; OrderedLocusNames=CV_0611; OS Chromobacterium violaceum. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Chromobacterium. OX NCBI_TaxID=536; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12472 / DSM 30191 / IFO 12614 / JCM 1249 / NCIB 9131; RX MEDLINE=22882880; PubMed=14500782; DOI=10.1073/pnas.1832124100; RA Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., RA Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., RA Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., RA Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., RA Batista J.S., Belo A., van den Berg C., Bogo M., Bonatto S., RA Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., RA Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., RA Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., RA Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., RA Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., RA Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., RA Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., RA Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., RA Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., RA Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., RA di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., RA Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., RA Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., RA Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., RA Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., RA Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., RA Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., RA Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., RA Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., RA Vettore A., Wassem R., Zaha A., Simpson A.J.G.; RT "The complete genome sequence of Chromobacterium violaceum reveals RT remarkable and exploitable bacterial adaptability."; RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003). CC -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L- CC histidinol to L-histidinaldehyde and then to L-histidine (By CC similarity). CC -!- CATALYTIC ACTIVITY: L-histidinol + 2 NAD(+) = L-histidine + 2 CC NADH. CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016825; AAQ58287.1; -; Genomic_DNA. DR RefSeq; NP_900281.1; -. DR GeneID; 2548270; -. DR GenomeReviews; AE016825_GR; CV_0611. DR KEGG; cvi:CV_0611; -. DR NMPDR; fig|243365.1.peg.611; -. DR HOGENOM; Q7P0F6; -. DR BioCyc; CVIO243365:CV_0611-MON; -. DR GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:HAMAP. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_01024; -; 1. DR InterPro; IPR001692; Histidinol_DHase. DR InterPro; IPR012131; Hstdl_DHase_prok. DR PANTHER; PTHR21256:SF2; Hstdl_DH_prok; 1. DR Pfam; PF00815; Histidinol_dh; 1. DR PRINTS; PR00083; HOLDHDRGNASE. DR ProDom; PD002680; Histidinol_dh; 1. DR TIGRFAMs; TIGR00069; hisD; 1. DR PROSITE; PS00611; HISOL_DEHYDROGENASE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis; KW Metal-binding; NAD; Oxidoreductase; Zinc. FT CHAIN 1 434 Histidinol dehydrogenase. FT /FTId=PRO_0000135755. FT ACT_SITE 327 327 Proton acceptor (By similarity). FT ACT_SITE 328 328 Proton acceptor (By similarity). FT METAL 259 259 Zinc (By similarity). FT METAL 262 262 Zinc (By similarity). FT METAL 361 361 Zinc (By similarity). FT METAL 420 420 Zinc (By similarity). FT BINDING 130 130 NAD (By similarity). FT BINDING 191 191 NAD (By similarity). FT BINDING 214 214 NAD (By similarity). FT BINDING 237 237 Substrate (By similarity). FT BINDING 259 259 Substrate (By similarity). FT BINDING 262 262 Substrate (By similarity). FT BINDING 328 328 Substrate (By similarity). FT BINDING 361 361 Substrate (By similarity). FT BINDING 415 415 Substrate (By similarity). FT BINDING 420 420 Substrate (By similarity). SQ SEQUENCE 434 AA; 46030 MW; D240002A51339F53 CRC64; MLKLSSSQPD FAERLKALLA FETAQDPAVD AAVASICADV HHRGDAALVE HTNRFDRMQA AGMADLTLSR EQLEAAWLRL PADVRDALSA AAERVRRYHE KQLAHSWSYE DEDGTLLGQQ VTPLDRVGIY VPGGKAAYPS SVLMNALPAK VAGVGEIIMV VPTPGGERND LVLAAAYIAG VDKVFTVGGA QAVAALAYGT ETVPQVDKIT GPGNAYVAAA KRRVFGVVGI DMVAGPSEIL VICDGATDPD WVAMDLFSQA EHDEIAQAIL LCPSADYIAQ VEASIAKLLP SMPRRAIIEA SLAGRGALIQ VSDLAEACEI SNYIAPEHLE LSVADPDALL PQLRHAGAIF MGRFTSESLG DYCAGPNHVL PTSRTARFAS PLGVYDFQKR SSLIRVSQAG AQKLGRIASL LAHGEGLTAH ARAAELRLED GTPR //